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Anti-Fibrinogen Affibody®分子(ab31790)

概述

产品名称

Anti-Fibrinogen Affibody®分子

特异性

This Anti-Fibrinogen Affibody® Molecule is modified with a unique C-terminal cysteine for directed single-point chemical modification, facilitating coupling to matrices. However, tail-to-tail dimers are spontaneously generated via a disulphide bridge between the C-terminal cysteines. Prior to coupling via the C-terminal the Affibody® Molecule needs to be reduced to expose the reactive cysteine residue. Recommended reducing condition is 20mM DTT at a pH above 7.5 and incubation at room temperature for 2 hours. Remove excess DTT by passage through a desalting column, not by dialysis.

What are Affibody® Molecules?Affibody® affinity ligands are unique research reagents, produced using innovative protein-engineering technologies. They are small, simple proteins composed of a three-helix bundle based on the scaffold of one of the IgG-binding domains of Protein A. Protein A is a surface protein from the bacterium Staphylococcus aureus. This scaffold has excellent features as an affinity ligand and can be designed to bind with high affinity to any given target protein. The domain consists of 58 amino acids, 13 of which are randomized to generate Affibody® libraries with a large number of ligand variants. Thus, the libraries consist of a multitude of protein ligands with an identical backbone and variable surface-binding properties. In function, Affibody® Molecules mimic monoclonal antibodies. Compared to antibodies, the most striking dissimilarity of Affibody® Molecules is the small size. Affibody® Molecules have a molecular weight of 6kDa, compared to the molecular weight of antibodies, which is 150kDa. In spite of its small size, the binding site of Affibody® Molecules is similar to that of an antibody. The advantages of Affibody® Molcules over antibodies are: -their small size -the simple structure of the molecules -its robust physical properties; able to withstand a broad range of analytical conditions, including extreme pH and elevated temperature -its ability to fold correctly intracellularly -the fast and cost effective production in bacteria -the potential to couple Affibody® Molecules in multimeric constructs Affibody® Molecules have highly competitive properties for applications within affinity purification, sample preparation, protein detection and in vitro diagnostics.

性能

形式

Liquid

存放说明

Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term.

存储溶液

pH: 7.4Constituents: 0.079% Ammonium bicarbonate, PBS

Concentration information loading...

纯化说明

The purity of this product is >98% as determined by SDS-PAGE and RP-HPLC.

Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.

组织特异性

Plasma.

疾病相关

Defects in FGA are a cause of congenital afibrinogenemia (CAFBN) [MIM:202400]. This is a rare autosomal recessive disorder characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen. Note=The majority of cases of afibrinogenemia are due to truncating mutations. Variations in position Arg-35 (the site of cleavage of fibrinopeptide a by thrombin) leads to alpha-dysfibrinogenemias.Defects in FGA are a cause of amyloidosis type 8 (AMYL8) [MIM:105200]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.

序列相似性

Contains 1 fibrinogen C-terminal domain.

结构域

A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure.

翻译后修饰

The alpha chain is not glycosylated.Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers.About one-third of the alpha chains in the molecules in blood were found to be phosphorylated.Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers.Phosphorylation sites are present in the extracellular medium.

Anti-Fibrinogen Affibody® Molecule 图像

ELISA - Anti-Fibrinogen Affibody® Molecule (ab31790)

The Anti-Fibrinogen Affibody® molecule can be used as capture reagent in a sandwich ELISA in combination with a goat anti-fibrinogen antibody as the detection reagent. Titration of fibrinogen gives a sigmoid curve with a sensitivity of 2.0 ng fibrinogen/ml (defined as two times background value).